Fluorescence method for enzyme analysis which couples aromatic amines with aromatic aldehydes
Abstract
Analysis of proteinases is accomplished using conventional amino acid containing aromatic amine substrates. Aromatic amines such as 4-methoxy-2-naphthylamine (4M2NA), 2-naphthylamine, aminoisophthalic acid dimethyl ester, p-nitroaniline, 4-methoxy-1-aminofluorene and coumarin derivatives resulting from enzymatic hydrolysis of the substrate couples with aromatic aldehydes such as 5-nitrosalicylaldehyde (5-NSA), benzaldehyde and p-nitrobenzaldehyde to produce Schiff-base complexes which are water insoluble. Certain Schiff-base complexes produce a shift from blue to orange-red (visible) fluorescence. Such complexes are useful in the assay of enzymes.
- Inventors:
-
- 557 Escondido Cir., Livermore, CA 94550
- 5178 Diane La., Livermore, CA 94550
- Issue Date:
- Research Org.:
- Lawrence Livermore National Laboratory (LLNL), Livermore, CA (United States)
- OSTI Identifier:
- 863690
- Patent Number(s):
- 4229528
- Assignee:
- Smith, Robert E. (557 Escondido Cir., Livermore, CA 94550);Dolbeare, Frank A. (5178 Diane La., Livermore, CA 94550)
- Patent Classifications (CPCs):
-
C - CHEMISTRY C12 - BIOCHEMISTRY C12Q - MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS
- DOE Contract Number:
- W-7405-ENG-48
- Resource Type:
- Patent
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; fluorescence; method; enzyme; analysis; couples; aromatic; amines; aldehydes; proteinases; accomplished; conventional; amino; acid; containing; amine; substrates; 4-methoxy-2-naphthylamine; 4m2na; 2-naphthylamine; aminoisophthalic; dimethyl; ester; p-nitroaniline; 4-methoxy-1-aminofluorene; coumarin; derivatives; resulting; enzymatic; hydrolysis; substrate; 5-nitrosalicylaldehyde; 5-nsa; benzaldehyde; p-nitrobenzaldehyde; produce; schiff-base; complexes; water; insoluble; shift; blue; orange-red; visible; useful; assay; enzymes; acid containing; aromatic amines; amino acid; enzymatic hydrolysis; water insoluble; aromatic aldehydes; enzyme analysis; fluorescence method; coumarin derivatives; ethyl ester; methyl ester; aromatic amine; amine substrates; conventional amino; couples aromatic; containing aromatic; PEPTIDE HYDROLASES; BIOASSAY; CHEMICAL ANALYSIS; HYDROLASES; LUMINESCENCE; ORGANIC COMPOUNDS; PROTEINS; /435/
Citation Formats
Smith, Robert E., and Dolbeare, Frank A. Fluorescence method for enzyme analysis which couples aromatic amines with aromatic aldehydes. United States: N. p., 1980.
Web.
Smith, Robert E., & Dolbeare, Frank A. Fluorescence method for enzyme analysis which couples aromatic amines with aromatic aldehydes. United States.
Smith, Robert E., and Dolbeare, Frank A. Tue .
"Fluorescence method for enzyme analysis which couples aromatic amines with aromatic aldehydes". United States. https://www.osti.gov/servlets/purl/863690.
@article{osti_863690,
title = {Fluorescence method for enzyme analysis which couples aromatic amines with aromatic aldehydes},
author = {Smith, Robert E. and Dolbeare, Frank A.},
abstractNote = {Analysis of proteinases is accomplished using conventional amino acid containing aromatic amine substrates. Aromatic amines such as 4-methoxy-2-naphthylamine (4M2NA), 2-naphthylamine, aminoisophthalic acid dimethyl ester, p-nitroaniline, 4-methoxy-1-aminofluorene and coumarin derivatives resulting from enzymatic hydrolysis of the substrate couples with aromatic aldehydes such as 5-nitrosalicylaldehyde (5-NSA), benzaldehyde and p-nitrobenzaldehyde to produce Schiff-base complexes which are water insoluble. Certain Schiff-base complexes produce a shift from blue to orange-red (visible) fluorescence. Such complexes are useful in the assay of enzymes.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Tue Oct 21 00:00:00 EDT 1980},
month = {Tue Oct 21 00:00:00 EDT 1980}
}
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